Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Clearing-factor lipase was assayed in acetone-ether-dried powders of heart and epididymal fat-pads of lean and genetically obese mice (ob/ob). In both tissues the enzyme activity in the adult was higher in the obese mice. 2. In heart the enzyme activity was unchanged from 8 to 48 weeks of age in lean mice, but in obese mice it increased between 8 and 12 weeks of age and remained elevated. 3. Starvation produced changes in the heart clearing-factor lipase activity in obese, but not lean, mice. 4. The clearing-factor lipase activity of epididymal fat-pads decreased rapidly during 24h starvation in both lean and obese mice, but the activity in the obese mice remained higher than that in lean mice. 5. Plasma triglyceride and cholesterol concentrations were determined in both lean and obese mice. Triglyceride concentrations were not greatly different, but the obese mice were hypercholesterolaemic. Plasma cholesterol concentrations were not correlated with changes in clearing-factor lipase activity.
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PMID:Clearing-factor lipase in obese hyperglycaemic mice (ob-ob). 464 30

1. When epididymal fat bodies from starved rats are incubated for 3.5hr. at 37 degrees in a defined medium in vitro the total clearing-factor lipase activity rises to approximately twice its initial value. 2. During the incubation period part of the tissue clearing-factor lipase activity appears in the medium. 3. Heparin, glucose, insulin, and HCO(3) (-) and K(+) ions are shown to be important medium constituents.
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PMID:Clearing-factor lipase in adipose tissue. A medium in which the enzyme activity of tissue from starved rats increases in vitro. 596 61

Norepinephrine-sensitive lipase activity was measured in rat epididymal fat pads by determining release either of free fatty acids or of glycerol. Stimulation of the lipase activity by norepinephrine in vitro could not be duplicated by injecting norepinephrine into the rats before sacrifice. A reliable method for assay of lipase deactivation rate was developed in which the tissue is incubated for 80 min, norepinephrine is added for a further incubation of 10 min, and the decay of lipase activity is measured during the next 10 min in the absence of hormone. Of the ketone bodies tested, -hydroxybutyrate and probably acetoacetate inhibited the activation of lipase by norepinephrine but had no effect on lipase deactivation rate, whereas acetone increased lipase activity stimulated by norepinephrine when tested at the concentration at which acetoacetate gave an inhibition. Substances other than -hydroxybutyrate that produce reduced nucleotides-alpha-glycerophosphate, malate, and ethanol-had no effect on lipase activity as tested in the present system.
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PMID:Effect of ketone bodies on lipolysis in adipose tissue in vitro. 597 Oct 44

The presence of a lipidbound inhibitor in adipose tissue of rats with hypothalamic obesity may explain the failure of the tissue to release fatty acids on epinephrine stinmulation. Aqueous extracts of tissue from obese animals showed no deficiency of lipase activity, but when whole homogenates of epididymal fat from lean and obese animals were mixed, 25 percent tissue from obese animals reduced by 73 percent the release expected from tissue of lean controls.
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PMID:Lipolysis in homogenates of adipose tissue: an inhibitor found in fat from obese rats. 600 38

When male rats were given single i.p. injection of 500 mg of L-arginine/100 g body weight, the pancreatic acinar cells were destroyed selectively, without any morphological change of Langerhans' islets. As early as 24 hours after the injection, loss of basophilia, zymogen degranulation, and vacuolar and necrotic changes of the acinar cells were noted. After 3 days, fibroblastic activity and atrophy of pancreatic lobuli were evident. Early electron microscopic findings were changes of the endoplasmic reticulum, such as partial dilatation or vacuolation of the cisternae, usually with loss of ribosomes attached to the membrane. The effect of arginine excess may be ascribed to imbalance of amino acids and subsequent to decrease of protein synthesis in the acinar cells. In the course of this study, fat necrosis with marked infiltration of leucocytes was observed in adipose tissues in peripancreatic, epididymal, omental and retroperitoneal areas. This change correlated closely with the marked necrosis of the pancreas. An increase in the level of lipase in the blood was also demonstrated.
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PMID:Effects of injecting excess arginine on rat pancreas. 619 86

A phosphoprotein phosphatase has been partially purified from rat epididymal fat pads by a procedure utilizing ammonium sulfate and ethanol precipitations and chromatography on DEAE-Sephadex A-50. The phosphatase was eluted from Sephadex G-75 columns with an apparent molecular weight of 28 000. The phosphoprotein phosphatase catalyzed the reversible deactivation of protein kinase activated chicken adipose tissue hormone-sensitive triglyceride lipase. Phosphatase activity measured with activated triglyceride lipase as substrate was completely dependent upon the presence of metal ions (Mg2+, Ca2+, or Mn2+) and was inhibited by inorganic phosphate and adenine nucleotides. The fat pad phosphatase increased the rate of activation of glycogen synthase in rat adipose tissue infranatant fractions from fed and 24-h fasted rats but had little or no effect on synthase activity in infranatant fractions from rats fasted for 48 h. Fasting had no effect on rat fat pad phosphatase activity measured with triglyceride lipase as substrate, but phosphatase activity was decreased in preparations from diabetic rats.
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PMID:Properties of a phosphoprotein phosphatase from rat epididymal fat pads: deactivation of hormone-sensitive triglyceride lipase and activation of glycogen synthase in adipose tissue. 624 77

Collagenase-treated isolated cells, prepared from epididymal fat pads of Sprague-Dawley rats exposed to 32Pi or (gamma-32P)-ATP, result in differences in label incorporation into peptides as determined by autoradiography of dried SDS polyacrylamide gels. 32Pi-labelled cells respond to epinephrine by increase in labeling of a 67,000-dalton band, presumably the activated lipase. (gamma-32P)-ATP exposed cells gave a dose-dependent increase in a 53,000-dalton band, a finding shared by cells exposed to cAMP in the absence of epinephrine. However, whereas, cAMP also significantly increased the labeling of an 18,000-dalton band, epinephrine had only a minor effect in the labeling of the 18,000-dalton component. Also, the degree of labeling of a 42,000-dalton band is diminished after epinephrine compared to unstimulated cells. By contrast, cAMP does not affect the labeling of the 42,000-dalton component. The localization of the 53,000- and the 18,000-dalton peptides as well as the enzyme(s) that catalyze their phosphorylation on the external surface of the fat cell is supported by studies using a number of macromolecular probes as well as by subcellular fractionation studies. The absence of such phosphopeptides or kinase activity in the infranatants of such cell suspensions eliminates the possibility that these phenomena are the result of leakage of cytoplasmic components. Thus, epinephrine appears to have effect and do not appear to be explicable simply by the release of cAMP to the extracellular compartment.
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PMID:Direct phosphorylation effects of epinephrine on the plasma membranes of intact rat fat cells. 626 72

Guinea pigs have varying plasma triglyceride concentrations ranging from 28 to 1392 mg/dl, with relatively uniform plasma cholesterol and phospholipid levels. To understand why the animals exhibit such wide variations of plasma triglyceride concentrations, we have explored the triglyceride hydrolyzing system by measuring tissue lipoprotein lipase activities and plasma activator for the enzyme. Lipoprotein lipase activities of epididymal adipose tissue of these animals were 759 +/- 117 (mean +/- SE) n moles FFA X min-1 X g wet tissue-1, markedly low compared with those of rats. There were no relationships between plasma triglyceride concentrations and tissue lipase activities. Plasma activator for lipoprotein lipase was lacking in this animal. Guinea pigs with ascorbic acid deficiency for 2 weeks also showed marked variations of plasma triglyceride concentrations, without any changes in tissue lipoprotein lipase activities. Low adipose tissue lipoprotein lipase activities with deficient plasma activator for the enzyme suggest that the lipoprotein lipase-mediated triglyceride degradation could be impaired in this animal, and this may account for the marked variation of plasma triglyceride concentrations.
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PMID:Wide variations of plasma triglyceride concentrations in guinea pigs. 652 15

Diurnal changes in glycogen stores of adipose tissues and in vitro lipolytic activity of isolated epididymal fat cells, and their lipolytic responsiveness to epinephrine and theophylline were examined in rats adapted to a 2-h daily meal feeding (20.00-22.00 h; darkness between 20.00-08.00 h) for 3 weeks and in control rats fed ad libitum. The fat cells from both groups of animals showed the peak of lipolytic activity at the mid-dark period (03.00 h), but the peak values and the average values at 6 or 7 time points examined within the 24-h feeding cycle were significantly higher (p less than 0.025) in meal-fed rats. Basal, epinephrine-stimulated, and epinephrine-induced lipolysis of fat cells from control rats showed diurnal changes, and the rhythms and their amplitude were affected by meal feeding. Changes in lipolytic activity of fat cells did not seem to relate directly to those of glycogen stores in adipose tissue. The over-all 24-h means of lipolytic activity of fat cells were significantly increased (p less than 0.001) with meal feeding. Mean cell size of epididymal fat pads was significantly smaller (p less than 0.001) in meal-fed rats, but lipolytic responsiveness to the graded concentrations of epinephrine and theophylline in the incubation medium was significantly greater (p less than 0.001) in meal-fed rats than in rats fed ad libitum. Thus, these findings suggest that lipolytic activity of the cAMP-hormone sensitive lipase system in fat cells might be increased with meal feeding in rats. Furthermore, the present results may give a new idea to consider the discrepancy that many workers have not been able to observe the increase in body fat deposition with meal feeding, which has been frequently reported to enhance lipogenesis in rats.
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PMID:Diurnal changes in lipolytic activity of isolated fat cells and their increased responsiveness to epinephrine and theophylline with meal feeding in rats. 668 56

Endothelial cells from rat epididymal fat pad capillaries were isolated from rats immediately after weaning. The cells were obtained after an initial brief incubation with collagenase under conditions of minimal breakage of cells. Adipocytes were removed by flotation and endothelial cells were then obtained as cell aggregates by fractional filtration procedures whereby intact tissue as well as free cells were removed. These aggregates were then dispersed and cultured in supplemented medium 199 whereby a monolayer of cells with a growth pattern, numerous pinocytotic vesicles, and intercellular junctions typical of endothelial cells were obtained. Minor contaminations of precursor cells to adipocytes were absent after one subculture. Here greater than 95% of the cells showed the presence of Factor VIII. Further subcultures produced nonhomogenous cells and decreasing rates of replication. The endothelial cells showed a very low rate of triglyceride synthesis and release, and collected no visible lipid upon prolonged cultures in the presence of an abundance of triglyceride substrate. They bound lipoprotein lipase from rat adipocytes, whereby the lipase was stabilized. This binding was released by heparin, and the cells did not synthesize the enzyme.
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PMID:Isolation and characterization of endothelial cells from the epididymal fat pad of the rat. 683 87


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